1MOW
E-DreI
1MOW の概要
| エントリーDOI | 10.2210/pdb1mow/pdb |
| 分子名称 | 5'-D(*CP*CP*AP*AP*AP*CP*TP*GP*TP*CP*TP*CP*AP*AP*GP*TP*TP*CP*CP*GP*GP*CP*G)-3', 5'-D(*CP*GP*CP*CP*GP*GP*AP*AP*CP*TP*TP*GP*AP*GP*AP*CP*AP*GP*TP*TP*TP*GP*G)-3', chimera of homing endonuclease I-DmoI and DNA endonuclease I-CreI, ... (7 entities in total) |
| 機能のキーワード | laglidadg, homing, engineering, design, endonuclease, hydrolase-dna complex, hydrolase/dna |
| 由来する生物種 | Desulfurococcus mobilis (,) 詳細 |
| 細胞内の位置 | Plastid, chloroplast: p05725 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 179359.22 |
| 構造登録者 | Chevalier, B.S.,Kortemme, T.,Chadsey, M.S.,Baker, D.,Monnat Jr., R.J.,Stoddard, B.L. (登録日: 2002-09-10, 公開日: 2002-11-29, 最終更新日: 2024-02-14) |
| 主引用文献 | Chevalier, B.S.,Kortemme, T.,Chadsey, M.S.,Baker, D.,Monnat Jr., R.J.,Stoddard, B.L. Design, Activity and Structure of a Highly Specific Artificial Endonuclease Mol.Cell, 10:895-905, 2002 Cited by PubMed Abstract: We have generated an artificial highly specific endonuclease by fusing domains of homing endonucleases I-DmoI and I-CreI and creating a new 1400 A(2) protein interface between these domains. Protein engineering was accomplished by combining computational redesign and an in vivo protein-folding screen. The resulting enzyme, E-DreI (Engineered I-DmoI/I-CreI), binds a long chimeric DNA target site with nanomolar affinity, cleaving it precisely at a rate equivalent to its natural parents. The structure of an E-DreI/DNA complex demonstrates the accuracy of the protein interface redesign algorithm and reveals how catalytic function is maintained during the creation of the new endonuclease. These results indicate that it may be possible to generate novel highly specific DNA binding proteins from homing endonucleases. PubMed: 12419232DOI: 10.1016/S1097-2765(02)00690-1 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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